6H9L
Kcr_0859 delta TM from Korarchaeum cryptofilum
6H9L の概要
エントリーDOI | 10.2210/pdb6h9l/pdb |
分子名称 | Uncharacterized protein (2 entities in total) |
機能のキーワード | coiled coil, beta-layer, membrane protein |
由来する生物種 | Korarchaeum cryptofilum (strain OPF8) |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 48999.35 |
構造登録者 | Hartmann, M.D.,Lupas, A.N.,Hernandez Alvarez, B. (登録日: 2018-08-04, 公開日: 2019-02-13, 最終更新日: 2024-11-13) |
主引用文献 | Adlakha, J.,Karamichali, I.,Sangwallek, J.,Deiss, S.,Bar, K.,Coles, M.,Hartmann, M.D.,Lupas, A.N.,Hernandez Alvarez, B. Characterization of MCU-Binding Proteins MCUR1 and CCDC90B - Representatives of a Protein Family Conserved in Prokaryotes and Eukaryotic Organelles. Structure, 27:464-475.e6, 2019 Cited by PubMed Abstract: Membrane-bound coiled-coil proteins are important mediators of signaling, fusion, and scaffolding. Here, we delineate a heterogeneous group of trimeric membrane-anchored proteins in prokaryotes and eukaryotic organelles with a characteristic head-neck-stalk-anchor architecture, in which a membrane-anchored coiled-coil stalk projects an N-terminal head domain via a β-layer neck. Based on sequence analysis, we identify different types of head domains and determine crystal structures of two representatives, the archaeal protein Kcr-0859 and the human CCDC90B, which possesses the most widespread head type. Using mitochondrial calcium uniporter regulator 1 (MCUR1), the functionally characterized paralog of CCDC90B, we study the role of individual domains, and find that the head interacts directly with the mitochondrial calcium uniporter (MCU) and is destabilized upon Ca binding. Our data provide structural details of a class of membrane-bound coiled-coil proteins and identify the conserved head domain of the most widespread type as a mediator of their function. PubMed: 30612859DOI: 10.1016/j.str.2018.11.004 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.19 Å) |
構造検証レポート
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